Mycobacterium tuberculosis DNA gyrase ATPase domain structures suggest a dissociative mechanism that explains how ATP hydrolysis is coupled to domain motion

Biochemical Journal

Volumn 456, Issue 2, 2013, Pages 263-273

  Agrawal, Alka ^a   Roué, Mélanie ^b,c,d   Spitzfaden, Claus ^a   Petrella, Stéphanie ^b,c,d   Aubry, Alexandra ^e,f,g   Hann, Michael ^a   Bax, Benjamin ^a   Mayer, Claudine ^b,c,d  

^a GLAXOSMITHKLINE   (United Kingdom)

^b INSTITUT PASTEUR   (France)

^c CNRS   (France)

^d UNIVERSITÉ PARIS DESCARTES   (France)

^e SORBONNE UNIVERSITÉ   (France)

^f PITIÉ SALPÊTRIÈRE HOSPITAL   (France)

^g Ctr Natl de Reference des Mycobacteries et de la Resistance des Mycobacteries Aux Antituberculeux   (France)

Author keywords

ATP hydrolysis; ATPase domain; Dissociative mechanism; DNA gyrase

Indexed keywords

ADENOSINE TRIPHOSPHATASE; ADENOSINE TRIPHOSPHATE; DIADENOSINE PENTAPHOSPHATE; DNA TOPOISOMERASE (ATP HYDROLYSING); GUANOSINE TRIPHOSPHATASE; NITROGEN; PHOSPHOTRANSFERASE;

ARTICLE; CRYSTAL STRUCTURE; CRYSTALLIZATION; DIMERIZATION; DISSOCIATION; HYDROGEN BOND; HYDROLYSIS; MYCOBACTERIUM TUBERCULOSIS; PRIORITY JOURNAL; PROTEIN DOMAIN; PROTEIN EXPRESSION; PROTEIN PURIFICATION; PROTEIN STRUCTURE;

ADENOSINE TRIPHOSPHATASES; ADENOSINE TRIPHOSPHATE; BACTERIAL PROTEINS; BIOCATALYSIS; CATALYTIC DOMAIN; CRYSTALLOGRAPHY, X-RAY; DNA GYRASE; DNA TOPOISOMERASES, TYPE II; HYDROGEN BONDING; HYDROLYSIS; MODELS, MOLECULAR; MYCOBACTERIUM TUBERCULOSIS; PROTEIN BINDING; PROTEIN STRUCTURE, SECONDARY; STRUCTURAL HOMOLOGY, PROTEIN;

EID: 84887448891     PISSN: 02646021     EISSN: 14708728     Source Type: Journal    
DOI: 10.1042/BJ20130538     Document Type: Article

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